Physiology of Microorganisms Lecture 1 PDF
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This document provides lecture notes on the physiology of microorganisms. It explores metabolic pathways, microbial growth mechanisms, and different types of enzymes. Concepts and classifications of enzymes are also covered, along with the lock-and-key and induced fit models of enzyme-substrate interactions.
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# Lecture 1: Physiology of Microorganisms - Exploring all metabolic and physiological pathways of microorganisms. ## Media and Microbial Growth - Media -> Microorganisms - Growth of Microorganisms: - Increase in cell biomass - Increase in cell number - Physiology: understanding the mecha...
# Lecture 1: Physiology of Microorganisms - Exploring all metabolic and physiological pathways of microorganisms. ## Media and Microbial Growth - Media -> Microorganisms - Growth of Microorganisms: - Increase in cell biomass - Increase in cell number - Physiology: understanding the mechanisms of microbial growth ## Media for Growing Fungi - Fungi contain: - Glucose (growth source) - Yeast extract or NaNO2 - MgSO4 - K2HPO4 - Micro-elements ## Composing Cell Biomass - **Polymers**: - Sugars - Starch - Cellulose - DNA - Protein - RNA **Note**: - The sugar resulted from microbial growth. - Chitin is the main component of fungal cell walls. - Cellulose is one of the most main components in most microorganisms. ## Enzymes - Natural proteins that accelerate or inactivate reactions by decreasing the energy required for the reaction. ## Enzyme Structure - **Holoenzyme:** - Protein (Apoenzyme) - Non-protein (Co-factor or Co-enzyme): - Metaloenzyme (metals like Cu, Fe, Zn) - Organic: - Vitamins - Fats - FAD, NAD - Heme - **The only case where enzymes don't compose from protein or contain only a low amount of protein is:** - **Ribozyme:** mainly RNA + few amount of protein. ## Enzyme Formation - **DNA** -> **Transcription** -> **RNA** -> **Translation** -> **Protein** ## Steps of Enzyme Maturation - **Start codon (AUG):** - Simple, encoding the protein - First amino acid is methionine - U terminal contains ammonia for methionine - **Maturation (Processing):** - Highly active enzyme ## Classification of Enzymes - Based on the International Union of Biochemistry (IUB). - Enzymes are classified into 6 categories based on 3 features: - Amino acid sequence - Sterio structure (orientation) of enzyme (molecular enzyme confirmation) - Catalysis (Type of catalysis) - According to the International Union of Biochemistry & Molecular Biology, the enzyme is described by an **enzymatic code**: - `EC X.X.X.X.` - `X` represents: - **Group Number**: [1-6] - **Sub-group**: [1-∞] - **Class**: Type of reaction - **Sub-class**: Type of substrate required co-factor ## 6 Categories of Enzymes - **1. Oxidoreductase enzymes (EC.1)** - Group of enzymes that do oxidation & reduction of two substrates at the same time. - Example: Respiration enzymes. - **2. Transferase enzyme (EC.2)** - The enzymes transfer a functional group from one substrate to another substrate. - **3- Hydrolase enzymes** - Hydrolysis of any bond of substrate using water. - **4. Lyase enzymes** - A group of enzymes (catalysis) that remove functional groups, resulting in unsaturated compounds (contain a double bond) - **5. Isomerase enzymes** - A group of enzymes that convert one compound to its isomer. - Example: - Ketone group to aldehyde group. - Double bond to single bond. - Glucose -> Fructose - **6- Ligase enzymes** - Ligation of simple molecules into large molecules. ## Example of Enzymatic Code: - `E.c. 4.1.1.11` - **Lyase**: - **Methionine** -> **Dethiolation (SH)** - **Deamination** (WH) - **Co-factor**: (vit b6) pyridoxine - **Type of substrate**: ## Enzyme Substrate Interaction - **1. Lock & key model (wrong theory)** - The enzyme combines with one absolute substrate. - **2. Induced. fit mechanism (model) (right theory)** - The active site of the enzyme and the substrate are more similar in sterioform/confirmation, the more affinity between them. ## Active Site - The binding between the active site and substrate is based on the orientation/structure/shape to fit the active site. ## Induced Fit Model - Enzyme can do re-orientation or adaptation to different substrates based on the similarities between substrates and active sites. - Chart: - Active site - S1: 100% affinity - S2: 50% affinity - S3: 0% affinity - Enzyme: - Non-active site - Alosteric site: Regulation of enzyme active site - The binding between the active site and substrate is based on the orientation/structure/shape to fit the active site.